Title : Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal.

Pub. Date : 1978 Nov 25

PMID : 711738






2 Functional Relationships(s)
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1 Treatment of free rhodanese with near-stoichiometric quantities of either iodoacetate or phenylglyoxal results in the rapid modification of the essential sulfhydryl group of Cys-247 and the consequent inactivation of the enzyme. Phenylglyoxal thiosulfate sulfurtransferase Bos taurus
2 Inactivation of free rhodanese by phenylglyoxal in the presence of cyanide was shown to be caused by a novel reaction in which disulfide bonds are formed between Cys-247 and either Cys-254 or Cys-263. Phenylglyoxal thiosulfate sulfurtransferase Bos taurus